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Author Kim, Keon Young ♦ Park*, Sangyoun
Source Directory of Open Access Journals (DOAJ)
Content type Text
Publisher Korean Society for Biochemistry and Molecular Biology
File Format HTM / HTML
Date Created 2013-01-22
Copyright Year ©2012
Language English
Subject Domain (in LCC) QH301-705.5 ♦ QD415-436
Subject Keyword Chemistry ♦ Biology ♦ Isothermal titration calorimetry ♦ PTB domain ♦ Organic chemistry ♦ Science ♦ Biochemistry ♦ IRAP ♦ Protein-protein interaction ♦ TBC1D4 (AS160)
Abstract Uptake of circulating glucose into the cells happens via the insulin-mediated signalling pathway, which translocates the glucosetransporter 4 (GLUT4) vesicles from the intracellular compartmentto the plasma membrane. RabㆍGTPases are involvedin this vesicle trafficking, where RabㆍGTPase-activatingproteins (RabGAP) enhance the GTP to GDP hydrolysis.TBC1D4 (AS160) and TBC1D1 are functional RabGAPs in theadipocytes and the skeletonal myocytes, respectively. Theseproteins contain two phosphotyrosine-binding domains (PTBs)at the amino-terminus of the catalytic RabGAP domain. Thesecond PTB has been shown to interact with the cytoplasmicregion of the insulin-regulated aminopeptidase (IRAP) of theGLUT4 vesicle. In this study, we quantitatively measured the∼μM affinity (KD) between TBC1D4 PTB and IRAP using isothermaltitration calorimetry, and further showed that IRAP residues1-49 are the major region mediating this interaction. Wealso demonstrated that the IRAP residues 1-15 are necessarybut not sufficient for the PTB interaction.
ISSN 1976670X
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG ♦ Career/Technical Study
Learning Resource Type Article
Publisher Date 2012-06-01
e-ISSN 19766696
Journal BMB Reports
Volume Number 45
Issue Number 6
Page Count 5
Starting Page 360
Ending Page 364


Source: Directory of Open Access Journals (DOAJ)